Microscale structural model of Alzheimer Aβ(1-40) amyloid fibril
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Buehler_Microscale structural.pdf
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Author(s)
Paparcone, Raffaella
Buehler, Markus J
Date Issued
June 2009
Journal
Applied Physics Letters
Publisher
American Institute of Physics (AIP)
Citation
Paparcone, Raffaella, and Markus J. Buehler. “Microscale Structural Model of Alzheimer Aβ(1–40) Amyloid Fibril.” Applied Physics Letters 94.24 (2009): 243904. © 2009 American Institute of Physics
Version
Final published version
Abstract
Amyloid fibril formation and characterization are crucial due to their association with severe degenerative disorders such as Alzheimer’s, type II diabetes, and Parkinson’s disease. Here we present an atomistic-based multiscale analysis, utilized to predict the structure of Alzheimer Aβ(1–40) fibrils. Our study provides a structural model of amyloid fibers with lengths of hundreds of nanometers at atomistic resolution. We report a systematic analysis of the energies, structural changes and H-bonding for varying fibril lengths, elucidating their size dependent properties. Our model predicts the formation of twisted amyloid microfibers with a periodicity of ≈82 nm, in close agreement with experimental results.
MIT Department
Massachusetts Institute of Technology. Department of Civil and Environmental Engineering
Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1063/1.3148641
